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Q16602

- CALRL_HUMAN

UniProt

Q16602 - CALRL_HUMAN

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Protein

Calcitonin gene-related peptide type 1 receptor

Gene
CALCRL, CGRPR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Receptor for calcitonin-gene-related peptide (CGRP) together with RAMP1 and receptor for adrenomedullin together with RAMP3 By similarity. Receptor for adrenomedullin together with RAMP2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.1 Publication

GO - Molecular functioni

  1. adrenomedullin receptor activity Source: UniProtKB
  2. calcitonin gene-related polypeptide receptor activity Source: Ensembl
  3. calcitonin receptor activity Source: Ensembl
  4. G-protein coupled receptor activity Source: ProtInc
  5. protein binding Source: UniProtKB
  6. protein transporter activity Source: UniProtKB

GO - Biological processi

  1. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: Ensembl
  2. angiogenesis Source: UniProtKB
  3. calcium ion transport Source: UniProtKB
  4. cAMP biosynthetic process Source: UniProtKB
  5. cellular response to sucrose stimulus Source: UniProtKB
  6. G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: ProtInc
  7. heart development Source: Ensembl
  8. negative regulation of inflammatory response Source: Ensembl
  9. positive regulation of cAMP biosynthetic process Source: UniProtKB
  10. positive regulation of smooth muscle cell proliferation Source: Ensembl
  11. protein transport Source: UniProtKB
  12. receptor internalization Source: UniProtKB
  13. regulation of muscle contraction Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_18290. Calcitonin-like ligand receptors.
REACT_19327. G alpha (s) signalling events.

Protein family/group databases

TCDBi9.A.14.4.12. the g-protein-coupled receptor (gpcr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcitonin gene-related peptide type 1 receptor
Short name:
CGRP type 1 receptor
Alternative name(s):
Calcitonin receptor-like receptor
Gene namesi
Name:CALCRL
Synonyms:CGRPR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:16709. CALCRL.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 146124Extracellular Reviewed predictionAdd
BLAST
Transmembranei147 – 16620Helical; Name=1; Reviewed predictionAdd
BLAST
Topological domaini167 – 1737Cytoplasmic Reviewed prediction
Transmembranei174 – 19320Helical; Name=2; Reviewed predictionAdd
BLAST
Topological domaini194 – 21320Extracellular Reviewed predictionAdd
BLAST
Transmembranei214 – 23623Helical; Name=3; Reviewed predictionAdd
BLAST
Topological domaini237 – 25317Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei254 – 27320Helical; Name=4; Reviewed predictionAdd
BLAST
Topological domaini274 – 28916Extracellular Reviewed predictionAdd
BLAST
Transmembranei290 – 31324Helical; Name=5; Reviewed predictionAdd
BLAST
Topological domaini314 – 33623Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei337 – 35418Helical; Name=6; Reviewed predictionAdd
BLAST
Topological domaini355 – 36612Extracellular Reviewed predictionAdd
BLAST
Transmembranei367 – 38822Helical; Name=7; Reviewed predictionAdd
BLAST
Topological domaini389 – 46173Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endosome Source: UniProtKB
  3. integral component of plasma membrane Source: ProtInc
  4. lysosome Source: UniProtKB
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi72 – 721W → A: Strongly reduced affinity for adrenomedullin. 1 Publication
Mutagenesisi92 – 921F → A: Strongly reduced affinity for adrenomedullin. 1 Publication
Mutagenesisi121 – 1211W → A: Strongly reduced affinity for adrenomedullin. 1 Publication

Organism-specific databases

PharmGKBiPA26033.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 461439Calcitonin gene-related peptide type 1 receptorPRO_0000012811Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi48 ↔ 742 Publications
Disulfide bondi65 ↔ 1052 Publications
Glycosylationi66 – 661N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi88 ↔ 1272 Publications
Glycosylationi118 – 1181N-linked (GlcNAc...) Reviewed prediction
Glycosylationi123 – 1231N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ16602.
PRIDEiQ16602.

PTM databases

PhosphoSiteiQ16602.

Expressioni

Tissue specificityi

Predominantly expressed in the lung and heart.

Gene expression databases

ArrayExpressiQ16602.
BgeeiQ16602.
CleanExiHS_CALCRL.
GenevestigatoriQ16602.

Organism-specific databases

HPAiHPA008070.

Interactioni

Subunit structurei

Heterodimer of CALCRL and RAMP3 By similarity. Heterodimer of CALCRL and RAMP1 or CALCRL and RAMP2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CALCAP068812EBI-962878,EBI-962928

Protein-protein interaction databases

BioGridi115498. 4 interactions.
DIPiDIP-37674N.
IntActiQ16602. 2 interactions.
STRINGi9606.ENSP00000376177.

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 5220
Beta strandi63 – 653
Beta strandi83 – 875
Beta strandi90 – 923
Beta strandi99 – 1057
Turni115 – 1173
Helixi125 – 1273
Helixi129 – 1313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AQFX-ray2.60B23-136[»]
3N7PX-ray2.80A/B/C/J23-133[»]
3N7RX-ray2.90A/B23-133[»]
3N7SX-ray2.10A/B23-133[»]
ProteinModelPortaliQ16602.
SMRiQ16602. Positions 36-132, 140-388.

Miscellaneous databases

EvolutionaryTraceiQ16602.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG255868.
HOVERGENiHBG102129.
InParanoidiQ16602.
KOiK04577.
OMAiLCWNDVA.
OrthoDBiEOG712TW2.
PhylomeDBiQ16602.
TreeFamiTF315710.

Family and domain databases

InterProiIPR003287. GCPR_2_calcitonin_rcpt_fam.
IPR017981. GPCR_2-like.
IPR003289. GPCR_2_CGRP1_rcpt.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSiPR01351. CGRPRECEPTOR.
PR01350. CTRFAMILY.
PR00249. GPCRSECRETIN.
SMARTiSM00008. HormR. 1 hit.
[Graphical view]
PROSITEiPS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q16602-1 [UniParc]FASTAAdd to Basket

« Hide

MEKKCTLNFL VLLPFFMILV TAELEESPED SIQLGVTRNK IMTAQYECYQ    50
KIMQDPIQQA EGVYCNRTWD GWLCWNDVAA GTESMQLCPD YFQDFDPSEK 100
VTKICDQDGN WFRHPASNRT WTNYTQCNVN THEKVKTALN LFYLTIIGHG 150
LSIASLLISL GIFFYFKSLS CQRITLHKNL FFSFVCNSVV TIIHLTAVAN 200
NQALVATNPV SCKVSQFIHL YLMGCNYFWM LCEGIYLHTL IVVAVFAEKQ 250
HLMWYYFLGW GFPLIPACIH AIARSLYYND NCWISSDTHL LYIIHGPICA 300
ALLVNLFFLL NIVRVLITKL KVTHQAESNL YMKAVRATLI LVPLLGIEFV 350
LIPWRPEGKI AEEVYDYIMH ILMHFQGLLV STIFCFFNGE VQAILRRNWN 400
QYKIQFGNSF SNSEALRSAS YTVSTISDGP GYSHDCPSEH LNGKSIHDIE 450
NVLLKPENLY N 461
Length:461
Mass (Da):52,929
Last modified:April 14, 2009 - v2
Checksum:iAF98E55E5454767C
GO

Sequence cautioni

The sequence BAF84319.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81N → Y.1 Publication
Corresponds to variant rs698577 [ dbSNP | Ensembl ].
VAR_054822
Natural varianti16 – 161F → L.
Corresponds to variant rs13391909 [ dbSNP | Ensembl ].
VAR_049453
Natural varianti274 – 2741R → I.
Corresponds to variant rs34010553 [ dbSNP | Ensembl ].
VAR_049454

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti144 – 1441L → Q in BAF84319. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L76380 mRNA. Translation: AAC41994.1.
U17473 mRNA. Translation: AAA62158.1.
AY389506 mRNA. Translation: AAQ91332.1.
AK291630 mRNA. Translation: BAF84319.1. Different initiation.
AK292998 mRNA. Translation: BAF85687.1.
AC007319 Genomic DNA. Translation: AAY14806.1.
AC074020 Genomic DNA. Translation: AAY14996.1.
CCDSiCCDS2293.1.
PIRiJC2477.
RefSeqiNP_001258680.1. NM_001271751.1.
NP_005786.1. NM_005795.5.
UniGeneiHs.470882.
Hs.744587.

Genome annotation databases

EnsembliENST00000392370; ENSP00000376177; ENSG00000064989.
ENST00000409998; ENSP00000386972; ENSG00000064989.
ENST00000410068; ENSP00000387190; ENSG00000064989.
GeneIDi10203.
KEGGihsa:10203.

Polymorphism databases

DMDMi226693507.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L76380 mRNA. Translation: AAC41994.1 .
U17473 mRNA. Translation: AAA62158.1 .
AY389506 mRNA. Translation: AAQ91332.1 .
AK291630 mRNA. Translation: BAF84319.1 . Different initiation.
AK292998 mRNA. Translation: BAF85687.1 .
AC007319 Genomic DNA. Translation: AAY14806.1 .
AC074020 Genomic DNA. Translation: AAY14996.1 .
CCDSi CCDS2293.1.
PIRi JC2477.
RefSeqi NP_001258680.1. NM_001271751.1.
NP_005786.1. NM_005795.5.
UniGenei Hs.470882.
Hs.744587.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3AQF X-ray 2.60 B 23-136 [» ]
3N7P X-ray 2.80 A/B/C/J 23-133 [» ]
3N7R X-ray 2.90 A/B 23-133 [» ]
3N7S X-ray 2.10 A/B 23-133 [» ]
ProteinModelPortali Q16602.
SMRi Q16602. Positions 36-132, 140-388.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115498. 4 interactions.
DIPi DIP-37674N.
IntActi Q16602. 2 interactions.
STRINGi 9606.ENSP00000376177.

Chemistry

BindingDBi Q16602.
ChEMBLi CHEMBL2111191.

Protein family/group databases

TCDBi 9.A.14.4.12. the g-protein-coupled receptor (gpcr) family.
GPCRDBi Search...

PTM databases

PhosphoSitei Q16602.

Polymorphism databases

DMDMi 226693507.

Proteomic databases

PaxDbi Q16602.
PRIDEi Q16602.

Protocols and materials databases

DNASUi 10203.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000392370 ; ENSP00000376177 ; ENSG00000064989 .
ENST00000409998 ; ENSP00000386972 ; ENSG00000064989 .
ENST00000410068 ; ENSP00000387190 ; ENSG00000064989 .
GeneIDi 10203.
KEGGi hsa:10203.

Organism-specific databases

CTDi 10203.
GeneCardsi GC02M188171.
HGNCi HGNC:16709. CALCRL.
HPAi HPA008070.
MIMi 114190. gene.
neXtProti NX_Q16602.
PharmGKBi PA26033.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG255868.
HOVERGENi HBG102129.
InParanoidi Q16602.
KOi K04577.
OMAi LCWNDVA.
OrthoDBi EOG712TW2.
PhylomeDBi Q16602.
TreeFami TF315710.

Enzyme and pathway databases

Reactomei REACT_18290. Calcitonin-like ligand receptors.
REACT_19327. G alpha (s) signalling events.

Miscellaneous databases

EvolutionaryTracei Q16602.
GeneWikii CALCRL.
GenomeRNAii 10203.
NextBioi 38620.
PROi Q16602.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16602.
Bgeei Q16602.
CleanExi HS_CALCRL.
Genevestigatori Q16602.

Family and domain databases

InterProi IPR003287. GCPR_2_calcitonin_rcpt_fam.
IPR017981. GPCR_2-like.
IPR003289. GPCR_2_CGRP1_rcpt.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view ]
Pfami PF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view ]
PRINTSi PR01351. CGRPRECEPTOR.
PR01350. CTRFAMILY.
PR00249. GPCRSECRETIN.
SMARTi SM00008. HormR. 1 hit.
[Graphical view ]
PROSITEi PS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A cDNA encoding the calcitonin gene-related peptide type 1 receptor."
    Aiyar N., Rand K., Elshourbagy N.A., Zeng Z., Adamou J.E., Bergsma D.J., Li Y.
    J. Biol. Chem. 271:11325-11329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cerebellum.
  3. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Kopatz S.A., Aronstam R.S., Sharma S.V.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TYR-8.
    Tissue: Placenta and Trachea.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-37.
  7. "Crystal structure of the ectodomain complex of the CGRP receptor, a class-B GPCR, reveals the site of drug antagonism."
    ter Haar E., Koth C.M., Abdul-Manan N., Swenson L., Coll J.T., Lippke J.A., Lepre C.A., Garcia-Guzman M., Moore J.M.
    Structure 18:1083-1093(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-133 IN COMPLEX WITH RAMP1 AND ANTAGONIST, SUBUNIT, DISULFIDE BONDS.
  8. "Structural basis for extracellular interactions between calcitonin receptor-like receptor and receptor activity-modifying protein 2 for adrenomedullin-specific binding."
    Kusano S., Kukimoto-Niino M., Hino N., Ohsawa N., Okuda K., Sakamoto K., Shirouzu M., Shindo T., Yokoyama S.
    Protein Sci. 21:199-210(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 23-136 IN COMPLEX WITH RAMP2, FUNCTION, MUTAGENESIS OF TRP-72; PHE-92 AND TRP-121, DISULFIDE BONDS.

Entry informationi

Entry nameiCALRL_HUMAN
AccessioniPrimary (citable) accession number: Q16602
Secondary accession number(s): A8K6G5
, A8KAD3, Q53S02, Q53TS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 14, 2009
Last modified: September 3, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi